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P28298

- ACEA_EMENI

UniProt

P28298 - ACEA_EMENI

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Protein

Isocitrate lyase

Gene

acuD

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Isocitrate = succinate + glyoxylate.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei206 – 2061

GO - Molecular functioni

  1. isocitrate lyase activity Source: ASPGD
  2. methylisocitrate lyase activity Source: ASPGD

GO - Biological processi

  1. acetate catabolic process Source: ASPGD
  2. carbon utilization Source: ASPGD
  3. fatty acid catabolic process Source: ASPGD
  4. glyoxylate cycle Source: UniProtKB-UniPathway
  5. propionate catabolic process, 2-methylcitrate cycle Source: ASPGD
  6. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glyoxylate bypass, Tricarboxylic acid cycle

Enzyme and pathway databases

UniPathwayiUPA00703; UER00719.

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate lyase (EC:4.1.3.1)
Short name:
ICL
Short name:
Isocitrase
Short name:
Isocitratase
Gene namesi
Name:acuD
ORF Names:AN5634
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560: Chromosome V

Subcellular locationi

GO - Cellular componenti

  1. glyoxysome Source: UniProtKB-KW
  2. peroxisomal matrix Source: ASPGD
  3. peroxisome Source: ASPGD
Complete GO annotation...

Keywords - Cellular componenti

Glyoxysome, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 538538Isocitrate lyasePRO_0000068790Add
BLAST

Expressioni

Inductioni

By acetate.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi162425.CADANIAP00003436.

Structurei

Secondary structure

1
538
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1614Combined sources
Helixi18 – 225Combined sources
Helixi25 – 295Combined sources
Helixi36 – 427Combined sources
Helixi52 – 6918Combined sources
Beta strandi73 – 775Combined sources
Helixi81 – 9010Combined sources
Beta strandi94 – 963Combined sources
Helixi98 – 1047Combined sources
Helixi122 – 14625Combined sources
Helixi150 – 1534Combined sources
Beta strandi165 – 1684Combined sources
Beta strandi173 – 1753Combined sources
Helixi176 – 18813Combined sources
Beta strandi192 – 1965Combined sources
Beta strandi212 – 2143Combined sources
Helixi217 – 23317Combined sources
Beta strandi239 – 2435Combined sources
Helixi246 – 2483Combined sources
Beta strandi249 – 2535Combined sources
Helixi258 – 2636Combined sources
Beta strandi264 – 2674Combined sources
Helixi275 – 28410Combined sources
Helixi290 – 30213Combined sources
Helixi309 – 3179Combined sources
Helixi324 – 33512Combined sources
Helixi340 – 35112Combined sources
Beta strandi369 – 3713Combined sources
Helixi375 – 38511Combined sources
Beta strandi390 – 3934Combined sources
Helixi401 – 41212Combined sources
Beta strandi419 – 4235Combined sources
Beta strandi426 – 4283Combined sources
Helixi430 – 4323Combined sources
Helixi436 – 4405Combined sources
Helixi442 – 4487Combined sources
Beta strandi451 – 4566Combined sources
Helixi459 – 47820Combined sources
Helixi480 – 4867Combined sources
Helixi488 – 4947Combined sources
Helixi497 – 4993Combined sources
Helixi501 – 5055Combined sources
Helixi507 – 51812Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DQUX-ray2.80A1-538[»]
ProteinModelPortaliP28298.
SMRiP28298. Positions 2-520.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28298.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2224.
HOGENOMiHOG000238475.
InParanoidiP28298.
KOiK01637.
OMAiALISHQF.
OrthoDBiEOG73Z331.

Family and domain databases

Gene3Di3.20.20.60. 2 hits.
InterProiIPR006254. Isocitrate_lyase.
IPR018523. Isocitrate_lyase_ph_CS.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERiPTHR21631:SF3. PTHR21631:SF3. 1 hit.
PfamiPF00463. ICL. 1 hit.
[Graphical view]
PIRSFiPIRSF001362. Isocit_lyase. 1 hit.
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR01346. isocit_lyase. 1 hit.
PROSITEiPS00161. ISOCITRATE_LYASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P28298-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSYIEEEDQR YWDEVAAVKN WWKDSRWRYT KRPFTAEQIV AKRGNLKIEY
60 70 80 90 100
PSNVQAKKLW GILERNFKNK EASFTYGCLD PTMVTQMAKY LDTVYVSGWQ
110 120 130 140 150
SSSTASSTDE PSPDLADYPM NTVPNKVNHL WMAQLFHDRK QREERMTTPK
160 170 180 190 200
DQRHKVANVD YLRPIIADAD TGHGGLTAVM KLTKLFVERG AAGIHIEDQA
210 220 230 240 250
PGTKKCGHMA GKVLVPISEH INRLVAIRAQ ADIMGTDLLA IARTDSEAAT
260 270 280 290 300
LITSTIDHRD HPFIIGSTNP DIQPLNDLMV MAEQAGKNGA ELQAIEDEWL
310 320 330 340 350
AKAGLKLFND AVVDAINNSP LPNKKAAIEK YLTQSKGKSN LEARAIAKEI
360 370 380 390 400
AGTDIYFDWE APRTREGYYR YQGGTQCAIN RAVAYAPFAD LIWMESKLPD
410 420 430 440 450
YKQAKEFADG VHAVWPEQKL AYNLSPSFNW KKAMPRDEQE TYIKRLGALG
460 470 480 490 500
YAWQFITLAG LHTTALISDT FAKAYAKQGM RAYGELVQEP EMANGVDVVT
510 520 530
HQKWSGANYV DNMLKMITGG VSSTAAMGKG VTEDQFKS
Length:538
Mass (Da):60,321
Last modified:May 1, 2007 - v3
Checksum:i21B5B56E5345681E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171Missing in CAA44572. (PubMed:1531185)Curated
Sequence conflicti68 – 681Missing in CAA44572. (PubMed:1531185)Curated
Sequence conflicti157 – 1571A → T in CAA44572. (PubMed:1531185)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62696 Genomic DNA. Translation: CAA44572.1.
AACD01000098 Genomic DNA. Translation: EAA62727.1.
BN001305 Genomic DNA. Translation: CBF81510.1.
PIRiS26857.
RefSeqiXP_663238.1. XM_658146.1.

Genome annotation databases

EnsemblFungiiCADANIAT00003436; CADANIAP00003436; CADANIAG00003436.
GeneIDi2871925.
KEGGiani:AN5634.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62696 Genomic DNA. Translation: CAA44572.1 .
AACD01000098 Genomic DNA. Translation: EAA62727.1 .
BN001305 Genomic DNA. Translation: CBF81510.1 .
PIRi S26857.
RefSeqi XP_663238.1. XM_658146.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DQU X-ray 2.80 A 1-538 [» ]
ProteinModelPortali P28298.
SMRi P28298. Positions 2-520.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 162425.CADANIAP00003436.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00003436 ; CADANIAP00003436 ; CADANIAG00003436 .
GeneIDi 2871925.
KEGGi ani:AN5634.2.

Phylogenomic databases

eggNOGi COG2224.
HOGENOMi HOG000238475.
InParanoidi P28298.
KOi K01637.
OMAi ALISHQF.
OrthoDBi EOG73Z331.

Enzyme and pathway databases

UniPathwayi UPA00703 ; UER00719 .

Miscellaneous databases

EvolutionaryTracei P28298.

Family and domain databases

Gene3Di 3.20.20.60. 2 hits.
InterProi IPR006254. Isocitrate_lyase.
IPR018523. Isocitrate_lyase_ph_CS.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view ]
PANTHERi PTHR21631:SF3. PTHR21631:SF3. 1 hit.
Pfami PF00463. ICL. 1 hit.
[Graphical view ]
PIRSFi PIRSF001362. Isocit_lyase. 1 hit.
SUPFAMi SSF51621. SSF51621. 1 hit.
TIGRFAMsi TIGR01346. isocit_lyase. 1 hit.
PROSITEi PS00161. ISOCITRATE_LYASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the glyoxysomal isocitrate lyase genes of Aspergillus nidulans (acuD) and Neurospora crassa (acu-3)."
    Gainey L.D.S., Connerton I.F., Lewis E.H., Turner G., Ballance D.J.
    Curr. Genet. 21:43-47(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: R153.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  4. "The crystal structure and active site location of isocitrate lyase from the fungus Aspergillus nidulans."
    Britton K.L., Langridge S.J., Baker P.J., Weeradechapon K., Sedelnikova S.E., De Lucas J.R., Rice D.W., Turner G.
    Structure 8:349-362(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Entry informationi

Entry nameiACEA_EMENI
AccessioniPrimary (citable) accession number: P28298
Secondary accession number(s): C8VFW4, Q5B1E6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: May 1, 2007
Last modified: November 26, 2014
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3